Summary: Please join us for a
Chemical Engineering Special Seminar
Thursday, March 15, 2012
346 Curry Student Center
11:45 a.m. ­ 1:25 p.m.
"Engineering New Strategies for the Treatment of Alzheimer's Disease"
THERESA A. GOOD, Ph.D.
Department of Chemical and Biochemical Engineering
University of Maryland Baltimore County (UMBC)
ABSTRACT
Alzheimer's disease is the leading cause of dementia in the aging population, affecting close to 30 million
people worldwide. One of the histopathological hallmarks of Alzheimer's disease is the deposition of insoluble
protein in the form of senile plaques. The primary protein component of these plaques is -amyloid, a 39 to 43
amino acid peptide which is able to self-assemble into amyloid fibrils. It is hypothesized by many that the
deposition of aggregated -amyloid (in fibril, protofibril, or oligomer form) is associated with neurotoxicity in the
diseases. In our laboratory, we are interested in understanding how this protein takes on its characteristic
amyloid structure, how size and structure are related to toxicity, and the interactions between the protein and
cells that lead to toxicity. To that end we have developed complementary experimental and modeling
approaches based on traditional chemical engineering analysis to gain insights into mechanisms of disease
and the role of protein structure in disease. Results from this work including computational protein-ligand